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Database: UniProt
Entry: A0A151JVC3_9HYME
LinkDB: A0A151JVC3_9HYME
Original site: A0A151JVC3_9HYME 
ID   A0A151JVC3_9HYME        Unreviewed;      2070 AA.
AC   A0A151JVC3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000256|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000256|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000256|HAMAP-Rule:MF_03001};
GN   ORFNames=ALC56_08214 {ECO:0000313|EMBL:KYN37426.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN37426.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN37426.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN37426.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN37426.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
CC       {ECO:0000256|HAMAP-Rule:MF_03001}.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03001}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001}.
CC   -!- SIMILARITY: Belongs to the IFT172 family.
CC       {ECO:0000256|ARBA:ARBA00038130}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000256|HAMAP-
CC       Rule:MF_03001}.
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DR   EMBL; KQ981706; KYN37426.1; -; Genomic_DNA.
DR   STRING; 34720.A0A151JVC3; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 1.25.40.470; -; 3.
DR   Gene3D; 1.25.40.980; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR15722; IFT140/172-RELATED; 1.
DR   PANTHER; PTHR15722:SF2; INTRAFLAGELLAR TRANSPORT PROTEIN 172 HOMOLOG; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF101898; NHL repeat; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03001};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_03001};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_03001}; Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_03001}; TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT   DOMAIN          64..149
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2070 AA;  232424 MW;  864D16D278B35004 CRC64;
     MAKKTQAEKT AQNDETVKGN DDPMNDDEEP NFSDPEGFVD DITDEELLGD ILKQKPSETD
     GVESVIVVDN VPRVEPDKLE KLQSVINKVL GKFGTIVNQY YPMNETDGKT KGYIFLEYNN
     HLNALTAVKS TNNYKIDKSH TFKVNLFTDF KKFEDIPENW EPPKAQPFKA ASDLHYHLLE
     PDAYDQFCVL CGNGAGVSVQ IWQNSAPEPT SLEERNRWTE TYVKWSPLGT YLSTFHKLGV
     ALWGGPQFTQ QARFSQRGVE CIDFSPCERY LVTYTPRTDL GQDQKRLVIW DILSGQEKRS
     FFPDGSSVWP IFRWSHDDKY LARMGEDILS VYETPSFGLL DKKSIKIPGI RDFSWSPTDN
     VLAYWVPEDK DVPARVTLLE IPNRNEIRNK NLFNVADCKI FWQKSGDYLC VKVDRFAKHY
     SHFTLQGMSY NFEIFHMREK QIPVDSVEIK EPIHAFAWEP VGSKFAIIHG EIPSVNVSFY
     EVRYGHQPAL LKRLEKKACN HLFWSPSGQF IVLAGLTTMA GALEFIDTND FTIMNSTDHY
     QTSDVEWDPT GRYVVTAVSS WKTSVDNGYW IWTFQGRILK RVNLTAFNQL LWRPRPPTLL
     TAEQIKEIKK NLKKYSAQFE SKDRMRLTRA SKFGKKSYLV KGIAFSPEST KIAVGQTDCI
     VYVYKIGEDW GDKKVICNKF RQSAAVTCLI WPVDGPIIVG LADGKVRAAM IKSQKTQTLY
     TSDAMTIALA SNVRGSGFLS GHADGSIIRY YIVEDGNAEP SGRVCVHGVP PYALAWPQSH
     ILAAGCDKRL TMYDPYGKPV KTFDFSRDFQ EREITVACCS PSGQSVAVGS WDKVRIFDWS
     PRRSIWEETN VRDLPNFYTV TALSWRRDGS KLIVGGLCGS VEQFETILRR TVVRGSHEVA
     YVGPSQVVIR PLSDSSQRPI VIRSQTGLEI EDVRVLGRRD NNVVARTART LLIGDIELGL
     ISEIPWEDRS GGEKFFFEYP VVCLIFCSGE LTIVEYGQNE ALGSVRTEAV NPHVVSVRVN
     ERLSSGGGDN KKLAYLLDPR TVRVIDLLSG ATISMIVHDA RIDWLELSEA GHKLLSRDKR
     GRLWLSDDEG DKVLLVTGVS FASWVTGSDV VVAQTGQTLA VWYNVDAPEA ITLTSIKGDV
     VDIVREDNRT SVMVEEHGGI KVAHQLDEGL IEFGTALHDN DFGRVILFLE NMGDGPQVET
     MWENVARNAM NERKLDIAAR CYAAMGDVAC AKFLKEIAEI GEKYAKETGN EPMANPECWA
     RLAVLNGDLK TAEAIYLEQN ELDKALDMYQ RYWRWEDALN LAESRSWSGL SELRDRHLAW
     LLDTGQAARA ASIIETTNPR RAVKLYLEAR RPGRAARLIL ADNELLEDER IVEEVISGLK
     ATDLAELAGE LLEKTGAGSE AIKCYSQAGV FARALDLARK IDPTLVVELE RDWGKHLSEN
     GHYDAAINHF IEAGETVLAL KAAINARQWR KALQIIQVIE DDNPEIRQQC EKLGEYFSSI
     GERSLAESLF IRAENAQRAV EIHIQSGDWI RAHQVAQEHM KSDEANQVLA KHAESLQQNG
     ELRHAESLYV AIGDHDAAIA MYRKAGNRSD MVRLVAQHRP DLLQTTHQHL ARELDAAGKA
     REAEEHFLGA GDWRGAVTAY RSANMWEDAL RVAKKASGEK AAQQVALMWA RTLAPELGAR
     LLMRLSYLEP CLQLACEANL FDWALEIAKY GTVDQKKEVH YRYAMALEDE GRFVEAEKEF
     VQAGKTMEAV QMYIHTRDWE SAEDVARSHS QEAVAQVLIA RAAEAAEGQD YATAEALLLR
     AHKPEMIIEH YKTAGMWSEA LRVCREYLPS QEAALRRELG QRSAGLDGAN ALEEARKWLN
     LGEVRPALDT LILNPQAPRS YLIRAADILL HQADPETAAE VGGDLGERLF SVGEHALAAQ
     KLNSCCQTAG SRAAAATAIT WSLNERLRIA DNVDKGCARR VSTIQYRNPP PTRETLGGEA
     RLYVHYVYTG TFLRNAKCRT LFGPFAKYPA DVIHPYEVSP RKLFGAFPRD FPYRPPPRLP
     SGFSAVAMNP LFLLTGVSVK PPVRRALALS
//
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